کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
70557 | 48837 | 2009 | 5 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Non-native states of cardosin A induced by acetonitrile: Activity modulation via polypeptide chains rearrangements
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کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
مهندسی شیمی
کاتالیزور
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چکیده انگلیسی
Cardosin A (EC: 3.4.23) is an enzyme containing two polypeptide chains, purified from pistils of Cynara cardunculus L., a cardoon, used for milk clotting in cheese making. It is a member of the aspartic proteinases (APs), like pepsin and HIV-proteinase that are composed by two symmetric units comprising the active site. Cardosin A is thought to be involved in many cellular events such as in pollen-pistil interaction and adhesion dependent recognition mechanisms. In the present study, the structural and activity effects of different amounts of acetonitrile (ACN) in cardosin A are presented. The results indicate that low ACN concentrations (up to 10% ACN) reversibly stimulate the enzyme activity accompanied by slight secondary structure induction. In light of the structural and stability studies performed so far, cardosin A can adopt conformational alterations that can result in activity modulation via polypeptide chains rearrangements.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Molecular Catalysis B: Enzymatic - Volume 61, Issues 3â4, December 2009, Pages 274-278
Journal: Journal of Molecular Catalysis B: Enzymatic - Volume 61, Issues 3â4, December 2009, Pages 274-278
نویسندگان
Cláudia S. Oliveira, A. Cristina Sarmento, Anabela Pereira, Isabel Correia, João Costa Pessoa, Valdemar I. Esteves, Henrique M.A.C. Fonseca, Euclides Pires, Marlene T. Barros,